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dc.contributor.authorHye Lim Kimen_US
dc.contributor.authorPreeyaporn Koedrithen_US
dc.contributor.authorSang Min Leeen_US
dc.contributor.authorYeo Jin Kimen_US
dc.contributor.authorYoung Rok Seoen_US
dc.contributor.otherDongguk University, Seoulen_US
dc.contributor.otherFaculty of Environment and Resource Studies, Mahidol Universityen_US
dc.date.accessioned2018-10-19T04:34:36Z-
dc.date.available2018-10-19T04:34:36Z-
dc.date.issued2013-11-01en_US
dc.identifier.citationMutation Research - Fundamental and Molecular Mechanisms of Mutagenesis. Vol.751-752, No.1 (2013), 1-7en_US
dc.identifier.issn09218262en_US
dc.identifier.issn00275107en_US
dc.identifier.other2-s2.0-84888057720en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84888057720&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/31176-
dc.description.abstractThioredoxin-1 (Trx1) is an antioxidant enzyme with a protective role in the removal of oxidative stress. We investigated the mechanism by which the redox modulator Trx1 affects base excision repair (BER) activity to understand the protective role of Trx1. We constructed a Trx1 knockdown system to demonstrate the specific mechanism of Trx1. DNA damage in terms of relative intensity of the DNA tail and γ-H2AX foci was markedly higher in the Trx1 shRNA cells compared with that in the wild type cells, leading to increased cellular susceptibility to a sublethal dose of BER-inducible toxicant, nitrosomethylurea (NMU). In addition, we observed a modulatory role of Trx1 in the BER pathway via the p53 downstream gene, growth arrest, and DNA-damage-inducible protein 45 α (Gadd45a). The protein level and function of p53, a Trx1 downstream gene, coincidently decreased in the Trx1 shRNA cells. Furthermore, Trx1 shRNA cells showed decreased Gadd45a expression and interaction of Gadd45a with apurinic/apyrimidinic endonuclease 1 (APE1) as well as APE1 activity. In conclusion, Trx1 might cooperate in the control of APE1 function by modulating the p53-mediated BER via the protein-protein interaction between Gadd45a and APE1, providing insight into the novel role of redox factor Trx1 in modulation of BER. © 2013 Elsevier B.V.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84888057720&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectEnvironmental Scienceen_US
dc.titleBase excision DNA repair defect in thioredoxin-1 (Trx1)-deficient cellsen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/j.mrfmmm.2013.10.002en_US
Appears in Collections:Scopus 2011-2015

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